Open AccessNeisseria gonorrhoeae possesses two nicotinamide adenine dinucleotide‐independent lactate dehydrogenases
Author(s) -
Fischer Randy S.,
Martin Gaines C.,
Rao Premila,
Jensen Roy A.
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb06611.x
Subject(s) - neisseria gonorrhoeae , biochemistry , nicotinamide adenine dinucleotide , cofactor , lactate dehydrogenase , nad+ kinase , isozyme , substrate (aquarium) , biology , esterase , chemistry , enzyme , microbiology and biotechnology , ecology
An important metabolic capability of Neisseria gonorrhoeae is the utilization of host‐derived lactate. Two isoenzymes of the membrane‐associated, pyridine dinucleotide‐independent type of lactate dehydrogenase (iLDH) participate in lactate assimilation, but exhibit distinctive properties. Isoenzyme iLDH‐I utilized lactate exclusively as substrate, exhibiting a preference for the D‐isomer. In contrast, isoenzyme iLDH‐II exhibited broad substrate specificity (lactate, phenyllactate, and 4‐hydroxyphenyllactate), but was stereospecific for the L‐isomers. These results explain the difficulty in isolating mutants unable to utilize lactate.